4oh3
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | + | ==Crystal structure of a nitrate transporter== | |
- | === | + | <StructureSection load='4oh3' size='340' side='right' caption='[[4oh3]], [[Resolution|resolution]] 3.25Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4oh3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH3 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NRT1.1, CHL1, NRT1, At1g12110, F12F1.1, T28K15_13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh3 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh3 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Nitrate is a primary nutrient for plant growth, but its levels in soil can fluctuate by several orders of magnitude. Previous studies have identified Arabidopsis NRT1.1 as a dual-affinity nitrate transporter that can take up nitrate over a wide range of concentrations. The mode of action of NRT1.1 is controlled by phosphorylation of a key residue, Thr 101; however, how this post-translational modification switches the transporter between two affinity states remains unclear. Here we report the crystal structure of unphosphorylated NRT1.1, which reveals an unexpected homodimer in the inward-facing conformation. In this low-affinity state, the Thr 101 phosphorylation site is embedded in a pocket immediately adjacent to the dimer interface, linking the phosphorylation status of the transporter to its oligomeric state. Using a cell-based fluorescence resonance energy transfer assay, we show that functional NRT1.1 dimerizes in the cell membrane and that the phosphomimetic mutation of Thr 101 converts the protein into a monophasic high-affinity transporter by structurally decoupling the dimer. Together with analyses of the substrate transport tunnel, our results establish a phosphorylation-controlled dimerization switch that allows NRT1.1 to uptake nitrate with two distinct affinity modes. | ||
- | + | Crystal structure of the plant dual-affinity nitrate transporter NRT1.1.,Sun J, Bankston JR, Payandeh J, Hinds TR, Zagotta WN, Zheng N Nature. 2014 Mar 6;507(7490):73-7. doi: 10.1038/nature13074. Epub 2014 Feb 26. PMID:24572362<ref>PMID:24572362</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
+ | [[Category: Arath]] | ||
[[Category: Bankston, J R.]] | [[Category: Bankston, J R.]] | ||
[[Category: Hinds, T R.]] | [[Category: Hinds, T R.]] |
Revision as of 12:38, 18 May 2014
Crystal structure of a nitrate transporter
|